Evidence map›Paper›PMID 33624332›Full record

ArticleChembiochem : a European journal of chemical biology2021

Biochemical Investigation of the Interaction of pICln, RioK1 and COPR5 with the PRMT5-MEP50 Complex.

Adrian Krzyzanowski, Raphael Gasper, Hélène Adihou, Peter 't Hart, Herbert Waldmann

Open access · hybridAbstract read
In one paragraph

Article in Chembiochem : a European journal of chemical biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.5field-weighted citation impact, top 18% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

16 citing papers in PubMed, 27 citations in OpenAlex.

  1. Article
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  7. Review
  8. Review
  9. Article
  10. Taming PRMT5-adaptor protein interactions.Trends in pharmacological sciences · 2023
    Article
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  14. Review
  15. Article
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 3 institutions in 3 countries.

Adrian KrzyzanowskiDepartment of Chemical Biology, Max Planck Institute of Molecular Physiology, Otto-Hahn-Strasse 11, 44227, Dortmund, Germany.
Raphael GasperCrystallography and Biophysics Unit, Max-Planck-Institute of Molecular Physiology, Otto-Hahn-Strasse 11, 44227, Dortmund, Germany.
Hélène AdihouAstraZeneca MPI Satellite Unit, Department of Chemical Biology, Max Planck Institute of Molecular Physiology, Otto-Hahn-Strasse 11, 44227, Dortmund, Germany.
Peter 't HartChemical Genomics Centre of the Max Planck Society, Max Planck Institute of Molecular Physiology, Otto-Hahn-Strasse 11, 44227, Dortmund, Germany.
Herbert WaldmannDepartment of Chemical Biology, Max Planck Institute of Molecular Physiology, Otto-Hahn-Strasse 11, 44227, Dortmund, Germany.ORCID 0000-0002-9606-7247
Max Planck Institute of Molecular Physiology · DETU Dortmund University · DEMax Planck Society · DE

Funding

Aventis FoundationStiftung Stipendien-Fonds of the Verbandes der Chemischen Industrie
6 · The paper itself

Abstract

The PRMT5-MEP50 methyltransferase complex plays a key role in various cancers and is regulated by different protein-protein interactions. Several proteins have been reported to act as adaptor proteins that recruit substrate proteins to the active site of PRMT5 for the methylation of arginine residues. To define the interaction between these adaptor proteins and PRMT5, we employed peptide truncation and mutation studies and prepared truncated protein constructs. We report the characterisation of the interface between the TIM barrel of PRMT5 and the adaptor proteins pICln, RioK1 and COPR5, and identify the consensus amino acid sequence GQF[D/E]DA[E/D] involved in binding. Protein crystallography revealed that the RioK1 derived peptide interacts with a novel PPI site.

Indexed as

Adaptor Proteins, Signal TransducingHumansProtein-Arginine N-MethyltransferasesProtein Processing, Post-TranslationalTranscription FactorsAdaptor Proteins, Signal TransducingPRMT5 protein, humanProtein-Arginine N-MethyltransferasesTranscription FactorsWDR77 protein, humaninterfacespeptidesprotein-protein interactionsproteins

Identifiers

PMID33624332
PMCPMC8252068
OpenAlexW3132972390

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.